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Cloning, Expression, and Characterization of a Novel Thermostable and Alkaline-stable Esterase from Stenotrophomonas maltophilia OUC_Est10 Catalytically Active in Organic Solvents.
- Source :
-
Catalysts (2073-4344) . May2019, Vol. 9 Issue 5, p401. 1p. - Publication Year :
- 2019
-
Abstract
- A thermostable and alkaline-stable novel esterase (Est7) was identified through the whole genome sequencing of Stenotrophomonas maltophilia OUC_Est10. The open reading frame of this gene encoded 617 amino acid residues. After heterologous expression in Escherichia coli BL21 (DE3), the purified Est7 was separated as a single protein and presented a molecular mass of 70.6 kDa. Multiple sequence alignment indicated that Est7 had a typical catalytic triad (Ser-Asp-His) and the conserved sequence (GDSL) typical of the family II lipid hydrolase proteins. Est7 showed good stability in alkaline buffers, especially in Tris-HCl buffer at pH 9.0 (residual activity 93.8% after 96 h at 4 °C) and in the medium temperature conditions (residual activity 70.2% after 96 h at 45 °C and pH 8.0). The enzyme also retained higher stability toward several hydrophilic and hydrophobic organic solvents (e.g., after incubation in 100% acetonitrile or in n-hexane the enzyme retained about 97% and 84% of the activity in the absence of organic solvent, respectively). Furthermore, Est7 could catalyze the transesterification reaction of vinylacetate with 2-phenylethanol and cis-3-hexen-1-ol to their corresponding acetate esters in petroleum ether or tert-butyl methyl ether. These results indicate Est7 as a promising biocatalyst for applications of Est7 in non-aqueous media. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 20734344
- Volume :
- 9
- Issue :
- 5
- Database :
- Academic Search Index
- Journal :
- Catalysts (2073-4344)
- Publication Type :
- Academic Journal
- Accession number :
- 136753783
- Full Text :
- https://doi.org/10.3390/catal9050401